ISCS_ECO57
ID ISCS_ECO57 Reviewed; 404 AA.
AC P0A6B9; P39171; P76581; P76992; Q8XA86;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000303|PubMed:20404999};
DE EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331};
GN Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331};
GN OrderedLocusNames=Z3797, ECs3396;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH TUSA OR APO-ISCU AND
RP PYRIDOXAL PHOSPHATE, FUNCTION, INTERACTION WITH CYAY; ISCU; ISCX; THII AND
RP TUSA, SUBUNIT, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-206, PATHWAY, AND
RP MUTAGENESIS OF ARG-39; TRP-45; GLU-49; ASP-52; ASP-65; PHE-89; ARG-112;
RP ARG-116; ARG-220; ARG-223; 223-ARG--ARG-225; 225-ARG--GLU-227; GLY-234;
RP 237-ARG--MET-239; GLU-311; ALA-327; CYS-328 AND ARG-340.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=20404999; DOI=10.1371/journal.pbio.1000354;
RA Shi R., Proteau A., Villarroya M., Moukadiri I., Zhang L., Trempe J.F.,
RA Matte A., Armengod M.E., Cygler M.;
RT "Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by
RT IscS protein-protein interactions.";
RL PLoS Biol. 8:E1000354-E1000354(2010).
CC -!- FUNCTION: Master enzyme that delivers sulfur to a number of partners
CC involved in Fe-S cluster assembly, tRNA modification or cofactor
CC biosynthesis (biotin, thiamine, molybdopterin). Catalyzes the removal
CC of elemental sulfur and selenium atoms from cysteine and selenocysteine
CC to produce alanine, then delivers the sulfur to an acceptor protein
CC such as CyaY, IscU, IscX, MoaD/MoeB, ThiI, or TusA. Transfers sulfur to
CC acceptor proteins via a transpersulfidation reaction; the flexibility
CC of the persulfide sulfur-carrying Cys-328 allows it to reach different
CC partners docked on the homodimer surface. May function as a selenium
CC delivery protein in the pathway for the biosynthesis of
CC selenophosphate. {ECO:0000269|PubMed:20404999}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00331};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000269|PubMed:20404999};
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00331, ECO:0000305|PubMed:20404999}.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with CyaY, IscU, IscX, ThiI
CC and TusA via an extended surface across both subunits centered around
CC Cys-328. The binding sites for different partners do not necessarily
CC overlap. Certain pairs of proteins can bind simultaneously to IscS;
CC IscS-IscU-CyaY and IscS-IscU-IscX complexes can be isolated in vitro,
CC but others (IscS-IscU-TusA, IscS-TusA-CyaY or IscS-IscX-TusA) complexes
CC cannot. {ECO:0000269|PubMed:20404999}.
CC -!- INTERACTION:
CC P0A6B9; Q8XAP0: cyaY; NbExp=2; IntAct=EBI-9011195, EBI-15850020;
CC P0A6B9; P0ACD6: iscU; NbExp=5; IntAct=EBI-9011195, EBI-9011202;
CC P0A6B9; P0C0M0: iscX; NbExp=2; IntAct=EBI-9011195, EBI-15849987;
CC P0A6B9; P0A892: tusA; NbExp=5; IntAct=EBI-9011195, EBI-15849930;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00331}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57644.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB36819.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57644.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36819.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_311423.2; NC_002695.1.
DR RefSeq; WP_001295373.1; NZ_SWKA01000005.1.
DR PDB; 3LVJ; X-ray; 2.44 A; A/B=1-404.
DR PDB; 3LVK; X-ray; 2.44 A; A=1-404.
DR PDB; 3LVL; X-ray; 3.00 A; B=1-404.
DR PDB; 3LVM; X-ray; 2.05 A; A/B=1-404.
DR PDBsum; 3LVJ; -.
DR PDBsum; 3LVK; -.
DR PDBsum; 3LVL; -.
DR PDBsum; 3LVM; -.
DR AlphaFoldDB; P0A6B9; -.
DR SMR; P0A6B9; -.
DR DIP; DIP-58573N; -.
DR IntAct; P0A6B9; 5.
DR STRING; 155864.EDL933_3693; -.
DR EnsemblBacteria; AAG57644; AAG57644; Z3797.
DR EnsemblBacteria; BAB36819; BAB36819; ECs_3396.
DR GeneID; 67416914; -.
DR GeneID; 915161; -.
DR KEGG; ece:Z3797; -.
DR KEGG; ecs:ECs_3396; -.
DR PATRIC; fig|386585.9.peg.3548; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_6; -.
DR OMA; KGLYWAR; -.
DR UniPathway; UPA00266; -.
DR EvolutionaryTrace; P0A6B9; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02006; IscS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridoxal phosphate; Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..404
FT /note="Cysteine desulfurase IscS"
FT /id="PRO_0000150265"
FT ACT_SITE 328
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT BINDING 75..76
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:20404999"
FT BINDING 155
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT BINDING 183
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:20404999"
FT BINDING 203..205
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:20404999"
FT BINDING 243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:20404999"
FT BINDING 328
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with IscU"
FT /note="via persulfide group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331,
FT ECO:0000269|PubMed:20404999"
FT MUTAGEN 39
FT /note="R->E: Decreased binding to CyaY."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 45
FT /note="W->R: No binding to TusA, decreased binding to ThiI.
FT 3% 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U), 7% 4-
FT thiouridine produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 49
FT /note="E->A: No binding to TusA. 24% mnm(5)s(2)U tRNA
FT produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 52
FT /note="D->A,M,R,Y: No binding to TusA. 0-20% mnm(5)s(2)U
FT tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 65
FT /note="D->F: Decreased binding to TusA. 22% mnm(5)s(2)U
FT tRNA produced."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 89
FT /note="F->E: Decreased binding to ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 112
FT /note="R->E: Decreased binding to IscX."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 116
FT /note="R->E: Decreased binding to CyaY, IscX, ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 220
FT /note="R->E: No binding to CyaY, IscX, ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 223..225
FT /note="RVR->EVE: No binding to IscX."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 223
FT /note="R->E: No binding CyaY, IscX, decreased binding to
FT ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 225..227
FT /note="RIE->EIR: No binding to CyaY, IscX."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 234
FT /note="G->L: Decreased binding to CyaY, IscX."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 237..239
FT /note="RGM->EGE: No binding to CyaY, IscX, ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 311
FT /note="E->R: Decreased binding to ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 327
FT /note="A->V: No binding to IscX, decreased binding to CyaY,
FT IscU, ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 328
FT /note="C->S: Retains binding to IscU, ThiI."
FT /evidence="ECO:0000269|PubMed:20404999"
FT MUTAGEN 340
FT /note="R->E: No binding to CyaY, ThiI, decreased binding to
FT IscX, TusA."
FT /evidence="ECO:0000269|PubMed:20404999"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 246..281
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3LVJ"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:3LVM"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3LVL"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:3LVM"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 363..381
FT /evidence="ECO:0007829|PDB:3LVM"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:3LVM"
SQ SEQUENCE 404 AA; 45090 MW; 1E4F2E6F9CD266B0 CRC64;
MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA VDIARNQIAD
LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS KTEHKAVLDT CRQLEREGFE
VTYLAPQRNG IIDLKELEAA MRDDTILVSI MHVNNEIGVV QDIAAIGEMC RARGIIYHVD
ATQSVGKLPI DLSQLKVDLM SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR
SGTLPVHQIV GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFSLGRF
TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE WAHH
